Pyruvate oxidase

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pyruvate oxidase
Identifiers
EC no. 1.2.3.3
CAS no. 9001-96-1
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
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NCBI proteins

In enzymology, a pyruvate oxidase (EC 1.2.3.3) is an enzyme that catalyzes the chemical reaction

pyruvate + phosphate + O2 acetyl phosphate + CO2 + H2O2

The 3 substrates of this enzyme are pyruvate, phosphate, and O2, whereas its 3 products are acetyl phosphate, CO2, and H2O2.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the aldehyde or oxo group of donor with oxygen as acceptor. The systematic name of this enzyme class is pyruvate:oxygen 2-oxidoreductase (phosphorylating). Other names in common use include pyruvic oxidase, and phosphate-dependent pyruvate oxidase. This enzyme participates in pyruvate metabolism. It has 2 cofactors: FAD, and Thiamin diphosphate.

Structural studies

As of late 2007, 12 structures have been solved for this class of enzymes, with PDB accession codes 1POW, 1POX, 1V5E, 1V5F, 1V5G, 1Y9D, 2DJI, 2EZ4, 2EZ8, 2EZ9, 2EZT, and 2EZU.

Related Research Articles

A dehydrogenase is an enzyme belonging to the group of oxidoreductases that oxidizes a substrate by reducing an electron acceptor, usually NAD+/NADP+ or a flavin coenzyme such as FAD or FMN. Like all catalysts, they catalyze reverse as well as forward reactions, and in some cases this has physiological significance: for example, alcohol dehydrogenase catalyzes the oxidation of ethanol to acetaldehyde in animals, but in yeast it catalyzes the production of ethanol from acetaldehyde.

Pyruvate dehydrogenase (NADP+) EC 1.2.1.51 is an enzyme that should not be confused with Pyruvate dehydrogenase (acetyltransferase) EC 1.2.4.1.

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References